PMID: 7030311Feb 1, 1981Paper

The use of naturally occurring hybrid variants of chloramphenicol acetyltransferase to investigate subunit contacts

The Biochemical Journal
L C Packman, W V Shaw

Abstract

1. Hybrids of the tetrameric enzyme chloramphenicol acetyltransferase (EC 2.3.1.28) were formed in vivo in a strain of Escherichia coli which harbours two different plasmids, each of which normally confers chloramphenicol resistance and specifies an easily distinguished enzyme variant (type I or type III) which is composed of identical subunits. Cell-free extracts of the dual-plasmid strain were found to contain five species of active enzyme, two of which were the homomeric enzymes corresponding to the naturally occurring tetramers of the type-I (beta 4) and type-III (alpha 4) enzymes. The other three variants were judged to be the heteromeric hybrid variants (alpha 3 beta, alpha 2 beta 2, alpha beta 3). 2. The alpha 3 beta and alpha 2 beta 2 hybrids of chloramphenicol acetyltransferase were purified to homogeneity by combining the techniques of affinity and ion-exchange chromatography. The alpha beta 3 variant was not recovered and may be unstable in vitro. 3. The unique lysine residues that could not be modified with methyl acetimidate in each of the native homomeric enzymes were also investigated in the heteromeric tetramers. 4. Lysine-136 remains buried in each beta subunit of the parental (type I) enzyme and in each of the...Continue Reading

Citations

Jan 1, 1983·CRC Critical Reviews in Biochemistry·W V Shaw
Aug 1, 1985·Antimicrobial Agents and Chemotherapy·M C RobertsJ H Crosa
Sep 22, 1982·Biochimica Et Biophysica Acta·J Müller, C Klein

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